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• W2047300521 startingPage "13063" @default.
• W2047300521 abstract "Significance Bone morphogenetic proteins (BMPs) are essential signaling molecules important in embryo development and maintaining tissue function in adulthood. BMPs are regulated outside the cell by inhibitors such as chordin. The structure of chordin is unknown as extracellular proteins are generally not suitable for high-resolution methods. This study uses electron microscopy and other techniques to determine the shape of human chordin. It has a compact horseshoe-shaped structure with the terminal BMP-binding regions protruding as prongs. The spacing of these domains supports a cooperative binding arrangement with BMPs. We compared BMP binding and inhibition by chordin with two truncated chordin variants. Proteolytic cleavage has little effect on binding of BMP-4 and BMP-7 but C-terminal cleavage makes chordin a better BMP inhibitor." @default.
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• W2047300521 date "2014-08-25" @default.
• W2047300521 modified "2023-10-01" @default.
• W2047300521 title "Nanoscale structure of the BMP antagonist chordin supports cooperative BMP binding" @default.
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• W2047300521 doi "https://doi.org/10.1073/pnas.1404166111" @default.
• W2047300521 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4246984" @default.
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